Molecular Machines

Hemoglobin

The 28 review prompts from the notes on Hemoglobin. Answer each in your head, then reveal it. Your grade decides when the card comes back.

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  1. What does hemoglobin carry, and from where to where?

  2. Hemoglobin spends no chemical fuel. What does the work of loading and unloading oxygen instead?

  3. Human adult hemoglobin has two alpha and two beta chains, arranged as a pair of blank.

  4. Why is hemoglobin's oxygen binding curve sigmoid?

  5. Unmodified, stroma-free human hemoglobin at pH 7.40 and 37 °C has a Hill coefficient of blank.

  6. Why does fetal hemoglobin hold oxygen more tightly than adult hemoglobin?

  7. In the global allostery model of hemoglobin, what carries much of the affinity change and most of the Bohr effect?

  8. Hemoglobin shows the minimum parts for an allosteric switch. What are the three parts?

  1. When the first oxygen binds a hemoglobin heme, the iron moves blank.

  2. In hemoglobin, what links the heme iron to the protein, so that the iron's move pulls on a helix?

  3. In hemoglobin, the blank contact is the switch point between the T and R quaternary states.

  4. When hemoglobin snaps from T to R, one alpha-beta dimer rotates by about blank against the other.

  5. Which three small molecules in working tissue push hemoglobin back toward the T state?

  6. Why does 2,3-BPG favour the T state of hemoglobin?

  7. Myoglobin has the same globin fold as hemoglobin. Why does myoglobin show no cooperativity?

  1. One human red blood cell holds about blank hemoglobin molecules.

  2. Why does a red blood cell not burn the oxygen its hemoglobin carries?

  3. Hemoglobin carries about blank of the oxygen in blood; the rest is dissolved.

  4. At rest, roughly what share of the oxygen delivered by hemoglobin do the body's tissues take?

  5. Hemoglobin is like a delivery van with four seats that loads and unloads as a team. Where does that analogy break?

  6. How does an approved Cas9 therapy use hemoglobin to treat sickle cell disease?

  1. Human blood under standard conditions (pH 7.4, pCO2 40 mmHg, 37 °C) has a P50 of blank.

  2. With a Hill coefficient of 2.8, by what factor must oxygen pressure rise to take hemoglobin from 10% to 90% saturation?

  3. Human hemoglobin has a Bohr coefficient of -0.29. What does a pH drop of 0.1 unit do to its P50?

  4. In crystals of human deoxyhemoglobin, how far does the heme iron sit from the porphyrin plane?

  5. When T-state hemoglobin crystals were oxygenated at all four hemes, what moved toward R while the tetramer stayed T?

  6. In R-state crystals of horse hemoglobin, what did the effector bezafibrate do to oxygen affinity?

  7. Cryo-EM puts liganded human hemoglobin, free of crystal contacts, closest to the blank quaternary arrangement.

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